Reference
Reference TypeLiterature
TitleImmunogenic HLA-DR-Presented Self-Peptides Identified Directly from Clinical Samples of Synovial Tissue, Synovial Fluid, or Peripheral Blood in Patients with Rheumatoid Arthritis or Lyme Arthritis.
AuthorsQi Wang; Elise E Drouin; Chunxiang Yao; Jiyang Zhang; Yu Huang; Deborah R Leon; Allen C Steere; Catherine E Costello
AffiliationsCenter for Biomedical Mass Spectrometry, Department of Biochemistry, Boston University School of Medicine , Boston, Massachusetts 02118, United States; Center for Immunology and Inflammatory Diseases, Division of Rheumatology, Allergy and Immunology, Massachusetts General Hospital, Harvard Medical School , Boston, Massachusetts 02114, United States; National University of Defense Technology , Changsha, 410000 Hunan Province, China.
JournalJ Proteome Res
Year2017
AbstractHuman leukocyte antigen-antigen D related (HLA-DR) molecules are highly expressed in synovial tissue (ST), the target of the immune response in chronic inflammatory forms of arthritis. Here, we used LC-MS/MS to identify HLA-DR-presented self-peptides in cells taken directly from clinical samples: ST, synovial fluid mononuclear cells (SFMC), or peripheral blood mononuclear cells (PBMC) from five patients with rheumatoid arthritis (RA) and eight with Lyme arthritis (LA). We identified 1593 non-redundant HLA-DR-presented peptides, derived from 870 source proteins. A total of 67% of the peptides identified in SFMC and 55% of those found in PBMC were found in ST, but analysis of SFMC/PBMC also revealed new antigen-presented peptides. Peptides were synthesized and examined for reactivity with the patients' PBMC. To date, three autoantigens in RA and four novel autoantigens in LA, presented in ST and/or PBMC, were shown to be targets of T- and B-cell responses in these diseases; ongoing analyses may add to this list. Thus, immunoprecipitation and LC-MS/MS can now identify hundreds of HLA-DR-presented self-peptides from individual patients' tissues or fluids with mixed cell populations. Importantly, identification of HLA-DR-presented peptides from SFMC or PBMC allows testing of more patients, including those early in the disease. Direct analysis of clinical samples facilitates identification of novel immunogenic T-cell epitopes.
Curation Last Updated2024-01-27 20:09:31
Epitope
Epitope ID593230
Chemical TypeLinear peptide
Linear SequenceVPVYFPAQDPRCDPK
Source Molecule NameArylsulfatase B
Source OrganismHomo sapiens (human)
Starting Position510
Ending Position524
Epitope Reference Details
Epitope Structure DefinesExact Epitope
Epitope NameVPVYFPAQDPRCDPK
Location of Data in ReferenceSupplementary Table 4
In Vivo Processing
Host OrganismHomo sapiens (human)
Host Details
Host Geolocationcontiguous United States of America
Age12 to 51 years
MHC Types presentHLA-DRB1*01:01;HLA-DRB1*04:01;HLA-DRB1*15:01
In Vivo Process
In Vivo Process TypeOccurrence of infectious disease
Disease StateLyme disease
Disease StageChronic;OGMS:0000064
In Vivo Processed Antigen
Epitope RelationOther
Object TypeOrganism
OrganismBorreliella burgdorferi (Lyme disease spirochete)
MHC Ligand Assay
Qualitative MeasurementPositive
Method/Techniquecellular MHC/mass spectrometry
Measurement ofligand presentation
Antigen Presenting Cells
Cell Tissue TypeOther
Cell TypeOther
Cell Culture ConditionsDirect Ex Vivo
MHC Allele
MHC Allele NameHLA-DR
MHC Evidence CodeElution with MHC specific antibody
MHC Ligand
Epitope RelationEpitope
Chemical TypeLinear peptide
Linear SequenceVPVYFPAQDPRCDPK
Source Molecule NameArylsulfatase B
Source OrganismHomo sapiens (human)
Starting Position510
Ending Position524
Assay Reference Details
Assay Comments by IEDB CuratorClinical samples of synovial tissue was used to identify HLA-DR presented self peptides.
Location of Assay Data in ReferenceSupplementary Table 4